1dk7

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{{STRUCTURE_1dk7| PDB=1dk7 | SCENE= }}
{{STRUCTURE_1dk7| PDB=1dk7 | SCENE= }}
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'''CRYSTAL STRUCTURE OF AN ISOLATED APICAL DOMAIN OF GROEL'''
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===CRYSTAL STRUCTURE OF AN ISOLATED APICAL DOMAIN OF GROEL===
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==Overview==
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The chaperonin GroEL is a double toriodal assembly that with its cochaperonin GroES facilitates protein folding with an ATP-dependent mechanism. Nonnative conformations of diverse protein substrates bind to the apical domains surrounding the opening of the double toroid's central cavity. Using phage display, we have selected peptides with high affinity for the isolated apical domain. We have determined the crystal structures of the complexes formed by the most strongly bound peptide with the isolated apical domain, and with GroEL. The peptide interacts with the groove between paired alpha helices in a manner similar to that of the GroES mobile loop. Our structural analysis, combined with other results, suggests that various modes of molecular plasticity are responsible for tight promiscuous binding of nonnative substrates and their release into the shielded cis assembly.
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(as it appears on PubMed at http://www.pubmed.gov), where 10619429 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10619429}}
==About this Structure==
==About this Structure==
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[[Category: Molecular chaperone]]
[[Category: Molecular chaperone]]
[[Category: Protein folding]]
[[Category: Protein folding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:11:42 2008''

Revision as of 20:11, 30 June 2008

Image:1dk7.png

Template:STRUCTURE 1dk7

CRYSTAL STRUCTURE OF AN ISOLATED APICAL DOMAIN OF GROEL

Template:ABSTRACT PUBMED 10619429

About this Structure

1DK7 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity., Chen L, Sigler PB, Cell. 1999 Dec 23;99(7):757-68. PMID:10619429

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